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Q8K4D7

- PLCZ1_MOUSE

UniProt

Q8K4D7 - PLCZ1_MOUSE

Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1

Gene

Plcz1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca2+-dependent manner. Triggers intracellular Ca2+ oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function.By similarity9 PublicationsCurated

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.By similarity

    Cofactori

    Calcium.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei178 – 1781By similarityPROSITE-ProRule annotation
    Active sitei223 – 2231By similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
    3. phospholipase C activity Source: MGI
    4. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. calcium ion transport Source: MGI
    2. egg activation Source: MGI
    3. intracellular signal transduction Source: InterPro
    4. lipid catabolic process Source: UniProtKB-KW
    5. multicellular organismal development Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Transducer

    Keywords - Biological processi

    Fertilization, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BRENDAi3.1.4.11. 3474.
    ReactomeiREACT_196473. Synthesis of IP3 and IP4 in the cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 (EC:3.1.4.11)
    Alternative name(s):
    Phosphoinositide phospholipase C-zeta-1
    Phospholipase C-zeta-1By similarity
    Short name:
    PLC-zeta-1By similarity
    Gene namesi
    Name:Plcz1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:2150308. Plcz1.

    Subcellular locationi

    Nucleus 5 Publications. Cytoplasmperinuclear region 5 Publications
    Note: Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis.5 Publications

    GO - Cellular componenti

    1. cytosol Source: InterPro
    2. nucleus Source: UniProtKB-SubCell
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi210 – 2101D → R: Defective in Ca(2+) oscillation activity and shows slower nuclear translocation. 1 Publication
    Mutagenesisi299 – 2991K → E: Defective in Ca(2+) oscillation activity and loss of nuclear translocation. 1 Publication
    Mutagenesisi301 – 3011K → E: Defective in Ca(2+) oscillation activity and loss of nuclear translocation. 1 Publication
    Mutagenesisi376 – 3761R → E: Abolishes nuclear translocation. 1 Publication
    Mutagenesisi377 – 3771K → E: Abolishes nuclear translocation. Prolongs Ca(2+) oscillations allowing them to occur during interphase. 2 Publications
    Mutagenesisi378 – 3781R → E: Abolishes nuclear translocation. 1 Publication
    Mutagenesisi379 – 3791K → E: Abolishes nuclear translocation. 1 Publication
    Mutagenesisi381 – 3811K → E: Abolishes nuclear translocation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6476471-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1PRO_0000347246Add
    BLAST

    Proteomic databases

    PRIDEiQ8K4D7.

    PTM databases

    PhosphoSiteiQ8K4D7.

    Expressioni

    Tissue specificityi

    Highly expressed in postpuberal testis, where expression is sperm cell-specific. Also expressed in brain of both sexes.1 Publication

    Gene expression databases

    BgeeiQ8K4D7.
    GenevestigatoriQ8K4D7.

    Interactioni

    Subunit structurei

    Interacts via its C2 domain with PtdIns3P and, to a lesser extent, PtdIns5P in vitro.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K4D7.
    SMRiQ8K4D7. Positions 26-642.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 7836EF-handPROSITE-ProRule annotationAdd
    BLAST
    Domaini163 – 307145PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini386 – 502117PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini507 – 610104C2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The EF-hand and C2 domains are essential for triggering Ca2+ oscillating activity and the regulation of PLCZ1 enzyme activity.4 Publications
    The X-Y linker region between PI-PLC X-box and Y-box domains may be a target for proteolysis and may play an important regulatory role during fertilization.4 Publications

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG149692.
    GeneTreeiENSGT00730000110266.
    HOGENOMiHOG000006871.
    HOVERGENiHBG053610.
    InParanoidiQ8K4D7.
    KOiK05861.
    OMAiMPEKDDF.
    OrthoDBiEOG7V49XT.
    PhylomeDBiQ8K4D7.
    TreeFamiTF313216.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    IPR001192. PI-PLC_fam.
    IPR017946. PLC-like_Pdiesterase_TIM-brl.
    IPR028395. PLC-zeta1.
    IPR015359. PLipase_C_EF-hand-like.
    IPR000909. PLipase_C_PInositol-sp_X_dom.
    IPR001711. PLipase_C_Pinositol-sp_Y.
    [Graphical view]
    PANTHERiPTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF29. PTHR10336:SF29. 1 hit.
    PfamiPF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    [Graphical view]
    PRINTSiPR00390. PHPHLIPASEC.
    SMARTiSM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 14 Publications (identifier: Q8K4D7-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MESQLHELAE ARWFLSKVQD DFRGGKINVE ITHKLLEKLD FPCHFAHVKH    50
    IFKENDRQNQ GRITIEEFRA IYRCIVHREE ITEIFNTYTE NRKILSENSL 100
    IEFLTQEQYE MEIDHSDSVE IINKYEPIEE VKGERQMSIE GFARYMFSSE 150
    CLLFKENCKT VYQDMNHPLS DYFISSSHNT YLISDQILGP SDIWGYVSAL 200
    VKGCRCLEID CWDGSQNEPI VYHGYTFTSK LLFKTVVQAI NKYAFVTSDY 250
    PVVLSLENHC SPGQQEVMAS ILQSTFGDFL LSDMLEEFPD TLPSPEALKF 300
    KILVKNRKVG TLSETHERIG TDKSGQVLEW KEVIYEDGDE DSGMDPETWD 350
    VFLSRIKEER EADPSTLSGI AGVKKRKRKM KIAMALSDLV IYTKAEKFRN 400
    FQYSRVYQQF NETNSIGESR ARKLSKLRVH EFIFHTAAFI TRVYPKMMRA 450
    DSSNFNPQEF WNVGCQMVAL NFQTPGLPMD LQNGKFLDNG GSGYILKPDI 500
    LRDTTLGFNP NEPEYDDHPV TLTIRIISGI QLPVSSSSNT PDIVVIIEVY 550
    GVPNDHVKQQ TRVVKNNAFS PKWNETFTFL IQVPELALIR FVVETQQGLL 600
    SGNELLGQYT LPVLCMNKGY RRVPLFSKSG ANLEPSSLFI YVWYFRE 647
    Length:647
    Mass (Da):74,614
    Last modified:October 1, 2002 - v1
    Checksum:iABE24E5CCCC63CA2
    GO
    Isoform 21 Publication (identifier: Q8K4D7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-110: Missing.

    Show »
    Length:537
    Mass (Da):61,307
    Checksum:i4B6832D35A65F75F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581Q → H in AAI06768. (PubMed:15489334)Curated
    Sequence conflicti360 – 3601R → K in AAI06768. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 110110Missing in isoform 2. 2 PublicationsVSP_052863Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF435950 mRNA. Translation: AAM95914.1.
    AK006672 mRNA. No translation available.
    BC106767 mRNA. Translation: AAI06768.1.
    CCDSiCCDS20671.1. [Q8K4D7-1]
    RefSeqiNP_473407.2. NM_054066.4. [Q8K4D7-1]
    XP_006506966.1. XM_006506903.1. [Q8K4D7-2]
    UniGeneiMm.50808.

    Genome annotation databases

    EnsembliENSMUST00000032356; ENSMUSP00000032356; ENSMUSG00000030230. [Q8K4D7-1]
    GeneIDi114875.
    KEGGimmu:114875.
    UCSCiuc009eny.1. mouse. [Q8K4D7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF435950 mRNA. Translation: AAM95914.1 .
    AK006672 mRNA. No translation available.
    BC106767 mRNA. Translation: AAI06768.1 .
    CCDSi CCDS20671.1. [Q8K4D7-1 ]
    RefSeqi NP_473407.2. NM_054066.4. [Q8K4D7-1 ]
    XP_006506966.1. XM_006506903.1. [Q8K4D7-2 ]
    UniGenei Mm.50808.

    3D structure databases

    ProteinModelPortali Q8K4D7.
    SMRi Q8K4D7. Positions 26-642.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8K4D7.

    Proteomic databases

    PRIDEi Q8K4D7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032356 ; ENSMUSP00000032356 ; ENSMUSG00000030230 . [Q8K4D7-1 ]
    GeneIDi 114875.
    KEGGi mmu:114875.
    UCSCi uc009eny.1. mouse. [Q8K4D7-1 ]

    Organism-specific databases

    CTDi 89869.
    MGIi MGI:2150308. Plcz1.

    Phylogenomic databases

    eggNOGi NOG149692.
    GeneTreei ENSGT00730000110266.
    HOGENOMi HOG000006871.
    HOVERGENi HBG053610.
    InParanoidi Q8K4D7.
    KOi K05861.
    OMAi MPEKDDF.
    OrthoDBi EOG7V49XT.
    PhylomeDBi Q8K4D7.
    TreeFami TF313216.

    Enzyme and pathway databases

    BRENDAi 3.1.4.11. 3474.
    Reactomei REACT_196473. Synthesis of IP3 and IP4 in the cytosol.

    Miscellaneous databases

    NextBioi 368899.
    PROi Q8K4D7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8K4D7.
    Genevestigatori Q8K4D7.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProi IPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    IPR001192. PI-PLC_fam.
    IPR017946. PLC-like_Pdiesterase_TIM-brl.
    IPR028395. PLC-zeta1.
    IPR015359. PLipase_C_EF-hand-like.
    IPR000909. PLipase_C_PInositol-sp_X_dom.
    IPR001711. PLipase_C_Pinositol-sp_Y.
    [Graphical view ]
    PANTHERi PTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF29. PTHR10336:SF29. 1 hit.
    Pfami PF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    [Graphical view ]
    PRINTSi PR00390. PHPHLIPASEC.
    SMARTi SM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PLC zeta: a sperm-specific trigger of Ca(2+) oscillations in eggs and embryo development."
      Saunders C.M., Larman M.G., Parrington J., Cox L.J., Royse J., Blayney L.M., Swann K., Lai F.A.
      Development 129:3533-3544(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6JImported.
      Tissue: Spermatid1 Publication.
    2. "Recombinant phospholipase Czeta has high Ca2+ sensitivity and induces Ca2+ oscillations in mouse eggs."
      Kouchi Z., Fukami K., Shikano T., Oda S., Nakamura Y., Takenawa T., Miyazaki S.
      J. Biol. Chem. 279:10408-10412(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Testis1 Publication.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis1 Publication.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Mammalian phospholipase Czeta induces oocyte activation from the sperm perinuclear matrix."
      Fujimoto S., Yoshida N., Fukui T., Amanai M., Isobe T., Itagaki C., Izumi T., Perry A.C.F.
      Dev. Biol. 274:370-383(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Cell cycle-dependent Ca2+ oscillations in mouse embryos are regulated by nuclear targeting of PLCzeta."
      Larman M.G., Saunders C.M., Carroll J., Lai F.A., Swann K.
      J. Cell Sci. 117:2513-2521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-377.
    7. "Nuclear translocation of phospholipase C-zeta, an egg-activating factor, during early embryonic development."
      Sone Y., Ito M., Shirakawa H., Shikano T., Takeuchi H., Kinoshita K., Miyazaki S.
      Biochem. Biophys. Res. Commun. 330:690-694(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta."
      Kouchi Z., Shikano T., Nakamura Y., Shirakawa H., Fukami K., Miyazaki S.
      J. Biol. Chem. 280:21015-21021(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, INTERACTION WITH PTDINS(3)P AND PTDINS(5)P, DOMAIN.
    9. "Role of phospholipase C-zeta domains in Ca2+-dependent phosphatidylinositol 4,5-bisphosphate hydrolysis and cytoplasmic Ca2+ oscillations."
      Nomikos M., Blayney L.M., Larman M.G., Campbell K., Rossbach A., Saunders C.M., Swann K., Lai F.A.
      J. Biol. Chem. 280:31011-31018(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    10. "The role of X/Y linker region and N-terminal EF-hand domain in nuclear translocation and Ca2+ oscillation-inducing activities of phospholipase Czeta, a mammalian egg-activating factor."
      Kuroda K., Ito M., Shikano T., Awaji T., Yoda A., Takeuchi H., Kinoshita K., Miyazaki S.
      J. Biol. Chem. 281:27794-27805(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF ASP-210; LYS-299; LYS-301; ARG-376; LYS-377; ARG-378; LYS-379 AND LYS-381.
    11. "Broad, ectopic expression of the sperm protein PLCZ1 induces parthenogenesis and ovarian tumours in mice."
      Yoshida N., Amanai M., Fukui T., Kajikawa E., Brahmajosyula M., Iwahori A., Nakano Y., Shoji S., Diebold J., Hessel H., Huss R., Perry A.C.
      Development 134:3941-3952(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, OVEREXPRESSION.
    12. "Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization."
      Kurokawa M., Yoon S.Y., Alfandari D., Fukami K., Sato K., Fissore R.A.
      Dev. Biol. 312:407-418(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    13. "Difference in Ca2+ oscillation-inducing activity and nuclear translocation ability of PLCZ1, an egg-activating sperm factor candidate, between mouse, rat, human, and medaka fish."
      Ito M., Shikano T., Oda S., Horiguchi T., Tanimoto S., Awaji T., Mitani H., Miyazaki S.
      Biol. Reprod. 78:1081-1090(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiPLCZ1_MOUSE
    AccessioniPrimary (citable) accession number: Q8K4D7
    Secondary accession number(s): Q3KPE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Transgenic mice, where broad ectopic expression is forced, initially appear healthy and their oocytes undergo unperturbed meiotic maturation to metaphase II but subsequently exhibit autonomous intracellular free calcium oscillations, second polar body extrusion, pronucleus formation and parthenogenetic development. Transgenic males remained largely asymptomatic, whereas transgenic females develop abdominal swellings caused by benign ovarian teratomas.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3